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- W2314605806 endingPage "527" @default.
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- W2314605806 abstract "Several human degenerative diseases involve amyloidogenic peptides/proteins with high conformational plasticity and propensity to self-aggregate into polymeric fibrillar assemblies sharing the cross-β structure and endowed with cytotoxic potential. Although the mechanisms of amyloid growth and toxicity are not fully understood, a common property of amyloids is their ability to interact with lipid bilayers disturbing membrane integrity. Lipid bilayers can also act as conformational catalysts, favoring protein misfolding and inducing the growth of aggregation nuclei, early oligomers, and mature fibrils with specific biophysical, structural, and toxicity features. This Perspective will highlight these effects in the context of a membrane-oligomer system where the conformational/biophysical features of either component affect those of the other. In this context, we will highlight the modulation of the protein-cell surface interaction by the content of membrane cholesterol and gangliosides, notably GM1. In particular, we will discuss data that indicate how these interactions affect the structural and stability properties of both protein and bilayers as well as the final cytotoxic effect. Our goal is to propose shared membrane-based mechanisms that could apply to any amyloidogenic peptide/protein, providing a biochemical background for amyloid growth and toxicity." @default.
- W2314605806 created "2016-06-24" @default.
- W2314605806 creator A5034128141 @default.
- W2314605806 creator A5079405830 @default.
- W2314605806 creator A5088431398 @default.
- W2314605806 date "2014-01-24" @default.
- W2314605806 modified "2023-10-01" @default.
- W2314605806 title "Amyloid Aggregation: Role of Biological Membranes and the Aggregate–Membrane System" @default.
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